Abstract：
:Ubiquitin C-terminal Hydrolase-1 (UCHL1) is a deubiquitinating enzyme, which plays a key role in Parkinson's disease (PD). It is one of the most important proteins, which constitute Lewy body in PD patient. However, how this well folded highly soluble protein presents in this proteinaceous aggregate is still unclear. We report here that UCHL1 undergoes S-nitrosylation in vitro and rotenone induced PD mouse model. The preferential nitrosylation in the Cys 90, Cys 152 and Cys 220 has been observed which alters the catalytic activity and structural stability. We show here that nitrosylation induces structural instability and produces amorphous aggregate, which provides a nucleation to the native α-synuclein for faster aggregation. Our findings provide a new link between UCHL1-nitrosylation and PD pathology.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Kumar R,Jangir DK,Verma G,Shekhar S,Hanpude P,Kumar S,Kumari R,Singh N,Sarovar Bhavesh N,Ranjan Jana N,Kanti Maiti Tdoi
10.1038/srep44558subject
Has Abstractpub_date
2017-03-16 00:00:00pages
44558issn
2045-2322pii
srep44558journal_volume
7pub_type
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